ID K5WVN1_AGABU Unreviewed; 834 AA.
AC K5WVN1;
DT 09-JAN-2013, integrated into UniProtKB/TrEMBL.
DT 09-JAN-2013, sequence version 1.
DT 27-MAR-2024, entry version 38.
DE RecName: Full=Phospholipase {ECO:0000256|PIRNR:PIRNR009376};
DE EC=3.1.4.4 {ECO:0000256|PIRNR:PIRNR009376};
GN ORFNames=AGABI1DRAFT_132820 {ECO:0000313|EMBL:EKM74848.1};
OS Agaricus bisporus var. burnettii (strain JB137-S8 / ATCC MYA-4627 / FGSC
OS 10392) (White button mushroom).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Agaricales; Agaricineae; Agaricaceae; Agaricus.
OX NCBI_TaxID=597362 {ECO:0000313|EMBL:EKM74848.1, ECO:0000313|Proteomes:UP000008493};
RN [1] {ECO:0000313|Proteomes:UP000008493}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JB137-S8 / ATCC MYA-4627 / FGSC 10392
RC {ECO:0000313|Proteomes:UP000008493};
RX PubMed=23045686; DOI=10.1073/pnas.1206847109;
RA Morin E., Kohler A., Baker A.R., Foulongne-Oriol M., Lombard V., Nagy L.G.,
RA Ohm R.A., Patyshakuliyeva A., Brun A., Aerts A.L., Bailey A.M.,
RA Billette C., Coutinho P.M., Deakin G., Doddapaneni H., Floudas D.,
RA Grimwood J., Hilden K., Kuees U., LaButti K.M., Lapidus A., Lindquist E.A.,
RA Lucas S.M., Murat C., Riley R.W., Salamov A.A., Schmutz J., Subramanian V.,
RA Woesten H.A.B., Xu J., Eastwood D.C., Foster G.D., Sonnenberg A.S.,
RA Cullen D., de Vries R.P., Lundell T., Hibbett D.S., Henrissat B.,
RA Burton K.S., Kerrigan R.W., Challen M.P., Grigoriev I.V., Martin F.;
RT "Genome sequence of the button mushroom Agaricus bisporus reveals
RT mechanisms governing adaptation to a humic-rich ecological niche.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:17501-17506(2012).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1,2-diacyl-sn-glycero-3-phosphocholine + H2O = a 1,2-diacyl-
CC sn-glycero-3-phosphate + choline + H(+); Xref=Rhea:RHEA:14445,
CC ChEBI:CHEBI:15354, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57643, ChEBI:CHEBI:58608; EC=3.1.4.4;
CC Evidence={ECO:0000256|PIRNR:PIRNR009376};
CC -!- SIMILARITY: Belongs to the phospholipase D family.
CC {ECO:0000256|PIRNR:PIRNR009376}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; JH971426; EKM74848.1; -; Genomic_DNA.
DR RefSeq; XP_007334520.1; XM_007334458.1.
DR AlphaFoldDB; K5WVN1; -.
DR STRING; 597362.K5WVN1; -.
DR GeneID; 18827774; -.
DR KEGG; abp:AGABI1DRAFT132820; -.
DR eggNOG; KOG1329; Eukaryota.
DR HOGENOM; CLU_000690_2_2_1; -.
DR InParanoid; K5WVN1; -.
DR OMA; VRHPHRE; -.
DR OrthoDB; 335467at2759; -.
DR Proteomes; UP000008493; Unassembled WGS sequence.
DR GO; GO:0070290; F:N-acylphosphatidylethanolamine-specific phospholipase D activity; IEA:UniProtKB-UniRule.
DR GO; GO:0004630; F:phospholipase D activity; IEA:UniProtKB-UniRule.
DR GO; GO:0035556; P:intracellular signal transduction; IEA:InterPro.
DR GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-KW.
DR GO; GO:0006654; P:phosphatidic acid biosynthetic process; IEA:InterPro.
DR CDD; cd09138; PLDc_vPLD1_2_yPLD_like_1; 1.
DR CDD; cd09141; PLDc_vPLD1_2_yPLD_like_2; 1.
DR Gene3D; 3.30.870.10; Endonuclease Chain A; 3.
DR InterPro; IPR025202; PLD-like_dom.
DR InterPro; IPR001736; PLipase_D/transphosphatidylase.
DR InterPro; IPR016555; PLipase_D_euk.
DR InterPro; IPR015679; PLipase_D_fam.
DR PANTHER; PTHR18896; PHOSPHOLIPASE D; 1.
DR PANTHER; PTHR18896:SF186; PHOSPHOLIPASE D; 1.
DR Pfam; PF00614; PLDc; 1.
DR Pfam; PF13091; PLDc_2; 1.
DR PIRSF; PIRSF009376; Phospholipase_D_euk; 3.
DR SMART; SM00155; PLDc; 2.
DR SUPFAM; SSF56024; Phospholipase D/nuclease; 2.
DR PROSITE; PS50035; PLD; 2.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PIRNR:PIRNR009376};
KW Lipid degradation {ECO:0000256|ARBA:ARBA00022963,
KW ECO:0000256|PIRNR:PIRNR009376};
KW Lipid metabolism {ECO:0000256|ARBA:ARBA00022963,
KW ECO:0000256|PIRNR:PIRNR009376};
KW Reference proteome {ECO:0000313|Proteomes:UP000008493}.
FT DOMAIN 176..203
FT /note="PLD phosphodiesterase"
FT /evidence="ECO:0000259|PROSITE:PS50035"
FT DOMAIN 620..647
FT /note="PLD phosphodiesterase"
FT /evidence="ECO:0000259|PROSITE:PS50035"
SQ SEQUENCE 834 AA; 96381 MW; F11DE00E3611AD0C CRC64;
MSMFTNAFTD AVKLVEKGVK HARAEAIGRF NPNRRHDEPE EQEQDRIRAE IRAGHRYESF
STVRTENFVK WHIDGHDYMW ALSEMLESAR EVIFILDWWL TPELYLRRPP AKYPEYRLDR
ILQRKAEQGV MIHVIVYKEV TQTMNMSSKH TKAKTLHPNI SCMRHPDHIG AKDSIEFWSH
HEKVVVVDNH YAAIGGLDLC FGRWDTHNHP LADVHPTDFS KTLFPGQDYN NARIMDFRDV
YNYASNQLSI LESARMPWHD VHMTFCGPVV LDVCQHFIER WNEIKKRKYR DEPRWPWLDL
PHKPEYAPEE AVARHPHLDK WRGIGRKYKQ RWHGLVDPDP EYPLPRNGTC TVQVVRSVSD
WSHGVLTEHS IQNAYLKMIE EAEHFIYIEN QFFISSTTDG DVVTNKIAKA LADRVIRAGQ
EGKRFKVVIF IPEVPGFAGN VKDEGSLKTI IGAQYRTINR GGNSIYEKVR EAGYEPLDYI
RFYHLRAYDR INAPLQYISQ TEDASGVKFF DAQVALSRKW VDGDMLTSQK TVQIKIPKET
TEGLVQSDQA GEDIQQLSIP ESEEQANETI TRFEEGAKSV RRDENVADNV VQHMLQDRTT
LAEEEWEGTE EEELNAYVTE LLYIHSKVMI VDDRRVIMGS ANINDRSQKG DGDSEICLVV
EDTDMIQSTM NGEPYDVSRF ASSLRRKLYR EHLGLIRPQM ADGCEEQTDF MQPAPLPNPD
ETGEEEDQLV ADPISEQTER LLRETAHSNR EIFSEIFKNV PTNVVRNWKT YDNYVPKVKT
GHVAPGITLD RLKEKLSRVR GAVVEAPLEF LIDESDLVSG AEWTSFNPTL PIYI
//
